Leonard Buckbinder

5.0k total citations · 1 hit paper
35 papers, 2.9k citations indexed

About

Leonard Buckbinder is a scholar working on Molecular Biology, Genetics and Immunology. According to data from OpenAlex, Leonard Buckbinder has authored 35 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 10 papers in Genetics and 9 papers in Immunology. Recurrent topics in Leonard Buckbinder's work include Neutrophil, Myeloperoxidase and Oxidative Mechanisms (6 papers), Cell Adhesion Molecules Research (6 papers) and Virus-based gene therapy research (5 papers). Leonard Buckbinder is often cited by papers focused on Neutrophil, Myeloperoxidase and Oxidative Mechanisms (6 papers), Cell Adhesion Molecules Research (6 papers) and Virus-based gene therapy research (5 papers). Leonard Buckbinder collaborates with scholars based in United States, Germany and Sweden. Leonard Buckbinder's co-authors include Bernd R. Seizinger, Nikolai Kley, Randy Talbott, Susana Velasco-Miguel, Ivone M. Takenaka, Barbara Faha, Donald D. Brown, Danny Reinberg, Juan M. Cárcamo and Yajun Mu and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Leonard Buckbinder

35 papers receiving 2.9k citations

Hit Papers

Induction of the growth inhibitor IGF-binding protein 3 b... 1995 2026 2005 2015 1995 200 400 600

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Leonard Buckbinder United States 24 1.7k 704 513 439 418 35 2.9k
Katherine T. Landschulz United States 13 1.3k 0.8× 477 0.7× 536 1.0× 369 0.8× 727 1.7× 17 3.3k
Gregory Hollis United States 36 2.7k 1.6× 1.0k 1.5× 369 0.7× 996 2.3× 390 0.9× 101 5.1k
Serge Hardy Canada 27 1.9k 1.1× 244 0.3× 387 0.8× 392 0.9× 235 0.6× 53 2.8k
Colin M. House Australia 29 3.3k 1.9× 532 0.8× 401 0.8× 341 0.8× 214 0.5× 48 4.0k
Lu‐Hai Wang United States 39 3.1k 1.8× 1.4k 2.0× 1.1k 2.2× 536 1.2× 321 0.8× 87 4.6k
Mark J. Evans United States 32 1.5k 0.9× 702 1.0× 276 0.5× 527 1.2× 233 0.6× 79 3.2k
Michiaki Kohno Japan 35 3.1k 1.8× 846 1.2× 531 1.0× 393 0.9× 128 0.3× 92 4.5k
Yiping Tu United States 26 2.0k 1.2× 466 0.7× 275 0.5× 240 0.5× 289 0.7× 53 3.1k
Carsten Jonat United States 5 2.6k 1.5× 798 1.1× 809 1.6× 797 1.8× 387 0.9× 8 4.2k
Hiroshi Shima Japan 35 3.0k 1.7× 599 0.9× 534 1.0× 388 0.9× 122 0.3× 141 4.0k

Countries citing papers authored by Leonard Buckbinder

Since Specialization
Citations

This map shows the geographic impact of Leonard Buckbinder's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Leonard Buckbinder with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Leonard Buckbinder more than expected).

Fields of papers citing papers by Leonard Buckbinder

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leonard Buckbinder. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Leonard Buckbinder. The network helps show where Leonard Buckbinder may publish in the future.

Co-authorship network of co-authors of Leonard Buckbinder

This figure shows the co-authorship network connecting the top 25 collaborators of Leonard Buckbinder. A scholar is included among the top collaborators of Leonard Buckbinder based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Leonard Buckbinder. Leonard Buckbinder is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Zeller, Matthias, Cuihua Wang, Edmund J. Keliher, et al.. (2023). Myeloperoxidase PET Imaging Tracks Intracellular and Extracellular Treatment Changes in Experimental Myocardial Infarction. International Journal of Molecular Sciences. 24(6). 5704–5704. 2 indexed citations
2.
Hedman, Åsa K., Camilla Hage, Anil Kumar Sharma, et al.. (2020). Identification of novel pheno-groups in heart failure with preserved ejection fraction using machine learning. Heart. 106(5). 342–349. 92 indexed citations
3.
Flach, Rachel J. Roth, Chunyan Su, Christian Cortés‐Campos, et al.. (2019). Myeloperoxidase inhibition in mice alters atherosclerotic lesion composition. PLoS ONE. 14(3). e0214150–e0214150. 35 indexed citations
4.
Wang, Cuihua, Edmund J. Keliher, Matthias Zeller, et al.. (2019). An activatable PET imaging radioprobe is a dynamic reporter of myeloperoxidase activity in vivo. Proceedings of the National Academy of Sciences. 116(24). 11966–11971. 33 indexed citations
6.
Eng, Heather, Raman Sharma, Angela Wolford, et al.. (2016). Species Differences in the Oxidative Desulfurization of a Thiouracil-Based Irreversible Myeloperoxidase Inactivator by Flavin-Containing Monooxygenase Enzymes. Drug Metabolism and Disposition. 44(8). 1262–1269. 8 indexed citations
7.
Ali, Muhammad, Benjamin Pulli, Gabriel Courties, et al.. (2016). Myeloperoxidase Inhibition Improves Ventricular Function and Remodeling After Experimental Myocardial Infarction. JACC Basic to Translational Science. 1(7). 633–643. 90 indexed citations
8.
Flach, Rachel J. Roth, Athanasia Skoura, Anouch Matevossian, et al.. (2015). Endothelial protein kinase MAP4K4 promotes vascular inflammation and atherosclerosis. Nature Communications. 6(1). 8995–8995. 88 indexed citations
9.
Nambiar, Prashant R., Gopinath S. Palanisamy, Carlin V. Okerberg, et al.. (2013). Toxicities Associated with 1-month Treatment with Propylthiouracil (PTU) and Methimazole (MMI) in Male Rats. Toxicologic Pathology. 42(6). 970–983. 23 indexed citations
10.
Tse, Kathy W.K., May Dang-Lawson, Angel Guzmán-Pérez, et al.. (2012). Small molecule inhibitors of the Pyk2 and FAK kinases modulate chemoattractant-induced migration, adhesion and Akt activation in follicular and marginal zone B cells. Cellular Immunology. 275(1-2). 47–54. 21 indexed citations
11.
Bonnette, Peter C., Brett S. Robinson, Jeffrey C. Silva, et al.. (2010). Phosphoproteomic characterization of PYK2 signaling pathways involved in osteogenesis. Journal of Proteomics. 73(7). 1306–1320. 36 indexed citations
12.
Tse, Kathy W.K., et al.. (2009). B Cell Receptor-induced Phosphorylation of Pyk2 and Focal Adhesion Kinase Involves Integrins and the Rap GTPases and Is Required for B Cell Spreading. Journal of Biological Chemistry. 284(34). 22865–22877. 37 indexed citations
13.
Han, Seungil, Anil Mistry, Jeanne S. Chang, et al.. (2009). Structural Characterization of Proline-rich Tyrosine Kinase 2 (PYK2) Reveals a Unique (DFG-out) Conformation and Enables Inhibitor Design. Journal of Biological Chemistry. 284(19). 13193–13201. 86 indexed citations
14.
Walker, Daniel P., Michael P. Zawistoski, Jiancheng Li, et al.. (2009). Sulfoximine-substituted trifluoromethylpyrimidine analogs as inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG activity. Bioorganic & Medicinal Chemistry Letters. 19(12). 3253–3258. 75 indexed citations
15.
Schaefer, Jean F., et al.. (2003). FGF signaling antagonizes cytokine-mediated repression of Sox9 in SW1353 chondrosarcoma cells. Osteoarthritis and Cartilage. 11(4). 233–241. 51 indexed citations
16.
Velasco-Miguel, Susana, Leonard Buckbinder, Randy Talbott, et al.. (1999). PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes. Oncogene. 18(1). 127–137. 207 indexed citations
17.
Neuberg, Manfred, Leonard Buckbinder, Bernd R. Seizinger, & Nikolai Kley. (1997). The p53/IGF-1 receptor axis in the regulation of programmed cell death. Endocrine. 7(1). 107–109. 28 indexed citations
18.
Buckbinder, Leonard & Donald D. Brown. (1993). Expression of the Xenopus laevis prolactin and thyrotropin genes during metamorphosis.. Proceedings of the National Academy of Sciences. 90(9). 3820–3824. 106 indexed citations
19.
20.
Nicholson, Wayne L., Glenn H. Chambliss, Leonard Buckbinder, Nicholas P. Ambulos, & Susan T. Lovett. (1985). Isolation and expression of a constitutive variant of the chloramphenicol-inducible plasmid gene cat-86 under control of the Bacillus subtilis 168 amylase promoter. Gene. 35(1-2). 113–120. 13 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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